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Database: UniProt
Entry: A0A0Q6PVT2_9MICO
LinkDB: A0A0Q6PVT2_9MICO
Original site: A0A0Q6PVT2_9MICO 
ID   A0A0Q6PVT2_9MICO        Unreviewed;       477 AA.
AC   A0A0Q6PVT2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:KQV06003.1};
GN   Name=manB {ECO:0000313|EMBL:KQV06003.1};
GN   ORFNames=ASC63_00425 {ECO:0000313|EMBL:KQV06003.1};
OS   Leifsonia sp. Root112D2.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leifsonia.
OX   NCBI_TaxID=1736426 {ECO:0000313|EMBL:KQV06003.1, ECO:0000313|Proteomes:UP000051914};
RN   [1] {ECO:0000313|EMBL:KQV06003.1, ECO:0000313|Proteomes:UP000051914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root112D2 {ECO:0000313|EMBL:KQV06003.1,
RC   ECO:0000313|Proteomes:UP000051914};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV06003.1, ECO:0000313|Proteomes:UP000051914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root112D2 {ECO:0000313|EMBL:KQV06003.1,
RC   ECO:0000313|Proteomes:UP000051914};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQV06003.1}.
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DR   EMBL; LMCU01000001; KQV06003.1; -; Genomic_DNA.
DR   RefSeq; WP_055808689.1; NZ_LMCU01000001.1.
DR   AlphaFoldDB; A0A0Q6PVT2; -.
DR   STRING; 1736426.ASC63_00425; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000051914; Unassembled WGS sequence.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03089; PMM_PGM; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR   Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR   InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR   InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR   InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR   InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR   InterPro; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR   PANTHER; PTHR43771:SF1; PHOSPHOMANNOMUTASE; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051914}.
FT   DOMAIN          16..128
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          169..270
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          292..389
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          395..476
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   477 AA;  50093 MW;  BDF631103CBA27B0 CRC64;
     MSSSARSIRA QLNAVVKSYD VRGLVGESLT AEIVTAIAAG FVDEVGAAGG DVVVGHDMRD
     SSPEFAAAFA AGAQARGANV VSIGLCSTDE SYYASGILNA PSAMFTASHN PATYNGIKLA
     RAGAQGISMQ TGLGTIRDRA EAYLTDGLVS TPAPGTFREQ NVLAGYAGYL RSLVDLSGIR
     PVTVVVDAGN GMGGLTVPAV LEEAAGLPAL PLTVIPLYFE LDGSFPNHEA NPLEPSNLVD
     LQKAVVQHGA DLGLAFDGDA DRCFVVDELG RAVTPSAVAA IVALREITRV RAADPDAEIT
     VLHNVITSNI VAETIEAAGA TAIRTKVGHS LIKDEMRATG AIFGGEHSAH YYFRDFWSAD
     NGMLAAMHLL AEFGTQDAPL SQLAERFDPY AGSGEINSTV ADVPAAYTRI VEAYSSIADL
     DEFDGLTVTG MVSPDEPFWW FSVRPSNTEP LLRLNVEAAD QPTMARIRDH VLALIRA
//
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